Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P02794 (ferritin)
 17,525 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A minor electrophoretically fast component was found in ferritin from iron-loaded rat liver in addition to a major electrophoretically slow ferritin similar to that observed in control rats. The electrophoretically fast ferritin showed immunological identity with the slow component, but on electrophoresis in SDS it gave a peptide of 17.3 kDa, in contrast with the electrophoretically slow ferritin, which gave a major band corresponding to the L-subunit (20.7 kDa). Thus the electrophoretically fast ferritin resembles that reported by Massover [(1985) Biochim. Biophys. Acta 829, 377-386] in livers of mice with short-term parenteral iron overload. The electrophoretically fast ferritin had a lower iron content (2000 Fe atoms/molecule) than the electrophoretically slow ferritin (3000 Fe atoms/molecule). Removal and re-incorporation of iron was possible without effect on the electrophoretic mobility of either ferritin species. On subcellular fractionation the electrophoretically fast ferritin was enriched in pellet fractions and was the sole soluble ferritin isolated from iron-laden secondary lysosomes (siderosomes). The amount and relative proportion of the electrophoretically fast species increased with iron loading. Haemosiderin isolated from siderosomes was found to contain a peptide reactive to anti-ferritin serum and corresponding to the 17.3 kDa peptide of the electrophoretically fast ferritin species. Unlike the electrophoretically slow ferritin, the electrophoretically fast ferritin did not become significantly radioactive in a 1 h biosynthetic labelling experiment. We conclude that the minor ferritin is not, as has been suggested for mouse liver ferritin, 'a completely new species of smaller holoferritin that represents a shift in the ferritin phenotype' in response to siderosis, but a precursor of haemosiderin, in agreement with the proposal by Richter [(1984) Lab. Invest. 50, 26-35] concerning siderosomal ferritin.
 ...
PMID:Siderosomal ferritin. The missing link between ferritin and haemosiderin? 366 70

Conjugated-Schiff's-base-type fluorescence was measured in iron-depleted samples and chloroform extracts of human spleen haemosiderin. Incubation of ferritin with liposomes and ascorbate led to the formation of compounds with similar fluorescence properties. Analysis of protein subunits by SDS/polyacrylamide-gel electrophoresis confirmed that ferritin was damaged in incubations with ascorbate. Since previous studies have shown that intact ferritin is resistant to proteolytic degradation, it is suggested that haemosiderin may be a product of oxidative reactions involving ferritin and lipid.
 ...
PMID:Haemosiderin-like properties of free-radical-modified ferritin. 382 50

Ferritin was purified from serum of patients with idiopathic haemochromatosis. Analysis on SDS electrophoresis showed that it is composed of two major bands of 19,000 and 23,000 Mr. The smaller peptide has an electrophoretic mobility and immunochemical reactivity similar to that of tissue L subunit. The larger, previously named G subunit, is recognized by concanavalin-A and by anti ferritin L-subunit, but not by anti-H, monoclonal antibodies. All of the antibodies show higher affinity for the L than for the G subunit. Therefore, the G chain appears immunochemically similar, but not identical, to ferritin L chain, and is responsible for serum ferritin binding concanavalin-A.
 ...
PMID:Human serum ferritin G-peptide is recognized by anti-L ferritin subunit antibodies and concanavalin-A. 382 32

The binding of human platelet cationic proteins (HuPlt CP) to rat renal cortex in vitro and in vivo, the loss of glomerular polyanions (GPA) and the increase in glomerular permeability were studied. HuPlt CP were purified by sequential cation-exchange chromatography and chromatofocusing, by which these proteins were shown to be highly cationic in nature (pI 10.5) and mainly composed of three molecular species of 55.60 kD, 40.45 kD, and 10 kD as studied by gel permeation in high pressure liquid chromatography and SDS-polyacrylamide gel electrophoresis. Binding of HuPlt CP to glomerular capillary walls (GCW), mesangium and to peritubular capillaries of the rat renal cortex was demonstrated by immunofluorescence, using a specific goat anti-HuPlt CP antiserum, after incubation of the sections with HuPlt CP in vitro and after injection of HuPlt CP in vivo. This interaction was ionic in nature, since treatment of sections with heparin abrogated the binding of HuPlt CP to glomerular structures. The glomerular deposits of HuPlt CP were associated with the loss of GPA as revealed by colloidal iron staining (light microscopy) in both in vitro and in vivo experiments and by ruthenium red staining (electron microscopy) in in vivo studies. After the injection of native ferritin, the increase in glomerular permeability produced by an infusion of HuPlt CP was observed by the increased ratio of counted particles within the glomerular basement membrane with respect to controls. The binding of HuPlt CP to GCW and the loss of GPA was consistent with the interpretation that HuPlt CP may increase glomerular permeability due to the neutralization of GPA.
 ...
PMID:Human platelet cationic proteins bind to rat glomeruli, induce loss of anionic charges and increase glomerular permeability. 400 94

A fluorescein- and lactoperoxidase-conjugated ferritin-anti-ferritin immune complex has been prepared for cell surface labeling experiments on immune recognition and effector function. Lactoperoxidase (LPO) has been covalently coupled to affinity-purified anti-ferritin antibodies with p-benzoquinone by a modified version of the method of Ternynck and Avrameas [Ternynck, T., & Avrameas, S. (1976) Ann. Immunol. (Paris) 127C, 197]. The conjugate is a heterodimer of Mr230 000 with linkages to either or both of the heavy and light chains of the antibody, as judged by two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) in the absence and presence of 2-mercaptoethanol. The conjugate retains antibody-binding activity as measured by a quantitative precipitin assay. When incorporated into immune complexes, the modified antibody also retains Fc receptor recognition ability as determined by erythrocyte-antibody rosette inhibition assays. Electron microscopy demonstrated that the antigen, ferritin, was monodisperse with complete apoprotein sheaths surrounding the core. Ferritin-anti-ferritin-LPO complexes were formed in 4-fold antigen excess. Complexes were verified by fluorescence and electron microscopy. Immune complexes were masked with "cold" iodine by use of the endogenous LPO activity. The complexes bound to cells at 4 degrees C as shown by electron microscopy and fluorescence video/intensification microscopy. The LPO delivered to the cell surface in this fashion can be utilized to iodinate the surface with 125I. Under saturation conditions, the labeling with local LPO delivery followed by SDS-PAGE and autoradiography is identical with labeling with free LPO. Labeling has also been conducted under conditions of substrate deficit.(ABSTRACT TRUNCATED AT 250 WORDS)
 ...
PMID:Macrophage recognition of immune complexes: development and application of novel cell surface labeling procedures. 405 86

Rhodopseudomonas viridis thylakoid membrane polypeptides were characterised by SDS gels, 2 D gels and surface-specific iodination. Four polypeptides with apparent molecular weights of 38 000, 33 000, 27 000, and 24 000 (reaction centre) and three low molecular weight polypeptides 11 000, 8000 and 6000 (probably light harvesting polypeptides) were identified. Antibodies were produced against the polypeptides eluted from SDS gels and tested for specificity by an immunoblotting assay. The antibodies were bound to the membranes and viewed by electron microscopy using a modification of the ferritin labelling technique. It is suggested that antigenic determinants for the 38 000, 33 000, and 27 000 reaction centre polypeptides and the 11 000 and 8000 low molecular weight polypeptides are present on the cytoplasmic membrane surface. The 33 000, 27 000, 11 000 and 6000 polypeptides appear to have surface-located residues which can be iodinated. The photosynthetic membrane of Rps. viridis appears to be a highly asymmetrical membrane.
 ...
PMID:Localisation of Rhodopseudomonas viridis reaction centre and light harvesting proteins using ferritin-antibody labelling. 618 15

The Con A-peroxidase reaction has demonstrated glycoproteins with molecular masses of 200 and 50 kilodalton on the polyacrylamide gel-SDS electrophoregrams of the molecular matrices isolated from rat liver, hepatoma 27 and Zajdela's ascites hepatoma. Both hepatomas contained an additional band of about 38 kilodalton, whereas Zajdela's hepatoma distinct bands of 54 kilodalton and less demonstrable of over 200 and about 105 and 68 kilodalton. Electron microscopy showed Con A-ferritin staining, more prominent in hepatomas than in the liver, at the periphery of isolated nuclear matrix preparations. Ruthenium red staining characteristic of acidic polysaccharides (glycosaminoglycans), on the contrary, was more pronounced in liver nuclear matrices.
 ...
PMID:[Carbohydrate components of the nuclear matrix in rat liver and hepatoma]. 619 9

Virus was isolated from infected mink organs by a combination of tissue homogenization, fluorocarbon extraction and ultracentrifugation. The final preparation was analysed by crossed immunoelectrophoresis and electronmicroscopy. Virions had a capsid diameter of 22 nm. Preparative agarose electrophoresis separated virions from contaminating ferritin. Crossed immunoelectrophoresis of virus gave a single precipitate with sera from infected mink. Crossed immunoelectrophoretic analysis with intermediate gels showed that a part of the virus preparation was complexed with antibody. Serum from a certain mink was found to contain precipitating antibody to (poly)nucleotid. Virus and virus-antibody complexes were found to focus at pH 4.0-4.4 in isoelectric focusing. In SDS-polyacrylamide gel-electrophoresis the main virus protein was found to have a molecular weight of 69000. This study gives further support to the classification of aleutian disease virus as a parvovirus.
 ...
PMID:Purification and characterization of Aleutian disease virus. 626 24

Isolated rat liver gap junctions were split by two methods. In the first method, isolated gap junctions were stabilized by cross-linking their cytoplasmic surfaces with glutaraldehyde under conditions that prevented the entry of glutaraldehyde into the "gap" region. The "stabilized" junctions were then split in the junctional gap with SDS. In the second procedure, unfixed gap junctions were split by incubation in urea-containing solutions. Junctional splitting was monitored by electron microscopy of thin sectioned and freeze fractured membrane pellets. Sidedness of the split junctional membranes was defined by labeling their cytoplasmic surfaces with glutaraldehyde-activated ferritin before splitting with urea. Gap junctional splitting did not result in any loss of protein components as determined by SDS-gel electrophoresis. The glutaraldehyde cross-linking procedure was also used to determine the effects of various detergents on the protein-protein interactions in the "gap" region. Of the detergents tested, only SDS caused junctional splitting.
 ...
PMID:Detergent sensitivity and splitting of isolated liver gap junctions. 642 4

Separation of the external membranes from freshly converted mechanical schistosomula of Schistosoma mansoni was achieved by osmotic shock under hypertonic conditions, followed by mechanical shearing and ultracentrifugation. Prior to treatment, the schistosomula were surface labeled by introduction of N-DNP-epsilon-aminocaproylphosphatidylethanolamine molecules into their lipid bilayer followed by anti-DNP antibodies and stained with either 125I-protein-A or ferritin labeled secondary anti-DNP antibodies. This label provided a membrane marker by which the purity of the preparation could be assessed at each stage. Fluorescence staining with FITC-conjugated secondary antibodies prior to treatment revealed that the homogeneously stained membrane of the intact schistosomula became swollen and ruptured after the osmotic shock. The isolated membrane pellet was intensely fluorescent. Electron microscopical examination revealed mostly vesicles, some of them with organized multilayer assembly. The vesicles were ferritin labeled, indicating that they originated from the outer surface membrane of the schistosomula. A 100 fold enrichment in the alkaline phosphatase activity and about 300 fold enrichment in acetylcholinesterase activity in the membrane preparations, as compared to the intact schistosomula, was found. The isolated tegument was analyzed by SDS-polyacrylamide gel electrophoresis. The pattern obtained showed three major bands, of molecular weights 69 000, 45 000 and 12 000 alongside with a large number of minor bands. Immunoprecipitation of the isolated 125I-labeled membrane antigens with antisera from chronically infected mice revealed these three major bands together with three other bands of molecular weight 38 000, 23 000 and 16 000.
 ...
PMID:Isolation and partial characterization of the tegumental outer membrane of schistosomula of Schistosoma mansoni. 652 92


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>